ID A1Z700_DROME Unreviewed; 1196 AA.
AC A1Z700;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE SubName: Full=Dilute class unconventional myosin, isoform B {ECO:0000313|EMBL:AAM68903.1};
GN Name=didum {ECO:0000313|EMBL:AAM68903.1,
GN ECO:0000313|FlyBase:FBgn0261397};
GN Synonyms=43CD {ECO:0000313|EMBL:AAM68903.1}, Didum
GN {ECO:0000313|EMBL:AAM68903.1}, Dmel\CG2146
GN {ECO:0000313|EMBL:AAM68903.1}, dmM5 {ECO:0000313|EMBL:AAM68903.1}, DmV
GN {ECO:0000313|EMBL:AAM68903.1}, M5 {ECO:0000313|EMBL:AAM68903.1}, Myo1C
GN {ECO:0000313|EMBL:AAM68903.1}, Myo5 {ECO:0000313|EMBL:AAM68903.1},
GN MYOV {ECO:0000313|EMBL:AAM68903.1}, MyoV
GN {ECO:0000313|EMBL:AAM68903.1}, myoV {ECO:0000313|EMBL:AAM68903.1},
GN MyoV43CD {ECO:0000313|EMBL:AAM68903.1}, NEST:bs14c05
GN {ECO:0000313|EMBL:AAM68903.1}, NMC7 {ECO:0000313|EMBL:AAM68903.1}, soy
GN {ECO:0000313|EMBL:AAM68903.1};
GN ORFNames=CG2146 {ECO:0000313|EMBL:AAM68903.1,
GN ECO:0000313|FlyBase:FBgn0261397}, Dmel_CG2146
GN {ECO:0000313|EMBL:AAM68903.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AAM68903.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AE013599; AAM68903.1; -; Genomic_DNA.
DR RefSeq; NP_724570.1; NM_165536.3.
DR AlphaFoldDB; A1Z700; -.
DR SMR; A1Z700; -.
DR IntAct; A1Z700; 3.
DR EnsemblMetazoa; FBtr0089744; FBpp0088685; FBgn0261397.
DR GeneID; 35680; -.
DR UCSC; CG2146-RB; d. melanogaster.
DR AGR; FB:FBgn0261397; -.
DR CTD; 35680; -.
DR FlyBase; FBgn0261397; didum.
DR VEuPathDB; VectorBase:FBgn0261397; -.
DR GeneTree; ENSGT00940000170389; -.
DR HOGENOM; CLU_000192_3_1_1; -.
DR OrthoDB; 1094820at2759; -.
DR BioGRID-ORCS; 35680; 0 hits in 3 CRISPR screens.
DR ChiTaRS; didum; fly.
DR GenomeRNAi; 35680; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261397; Expressed in thoracico-abdominal ganglion (Drosophila) and 26 other cell types or tissues.
DR ExpressionAtlas; A1Z700; baseline and differential.
DR Genevisible; A1Z700; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; ISS:FlyBase.
DR GO; GO:0031475; C:myosin V complex; IPI:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:FlyBase.
DR GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IPI:FlyBase.
DR GO; GO:0000146; F:microfilament motor activity; IDA:FlyBase.
DR GO; GO:0032027; F:myosin light chain binding; IPI:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IDA:FlyBase.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; HMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:FlyBase.
DR GO; GO:0045856; P:positive regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50096; IQ; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT DOMAIN 70..771
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 650..672
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 916..957
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 985..1085
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1150..1177
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1196 AA; 137916 MW; 3ED21A22CDA8272E CRC64;
MSSEEMLYAQ GAKIWVPHAD LVWESATLEE SYRKGAGFLK ICTDSGKLKE VKLKADGSDL
PPLRNPAILV GQNDLTTLSY LHEPGVLHNL RVRFCERQII YTYCGIILVA INPYAEMPLY
GPSIIRAYRG HAMGDLEPHI FALAEEAYTK LERENCNLSI IVSGESGAGK TVSAKYAMRY
FAAVGGSESE TQVERKVLAS SPIMEAFGNA KTTRNDNSSR FGKFTKLLFR NQMGVMFLQG
ATMHTYLLEK SRVVYQAQGE RNYHIFYQLC AARSKYPELV LDHQDKFQFL NMGGAPEIER
VSDAEQFNET VQAMTVLGFS IQQIADIVKI LAGILHLGNI QVSKKFNEGS EEEDSDSCDI
FHNDIHLQIT ADLLRVSADD LRRWLLMRKI ESVNEYVLIP NSIEAAQAAR DALAKHIYAK
LFQYIVGVLN KSLNNGSKQC SFIGVLDIYG FETFEVNSFE QFCINYANEK LQQQFNQHVF
KLEQEEYLKE GITWTMIDFY DNQPCIDLIE SRLGVLDLLD EECRMPKGSD ESWAGKLIGK
CNKFPHFEKP RFGTTSFFIK HFSDTVEYDV NGFLEKNRDT VSKELTQVLS ESNMSLAKQV
MTLEEIDTLC VDSAKSSTLG GRVVISAGRK QVVPSKQHRK TVGSQFQESL ASLISTLHAT
TPHYVRCIKP NDDKVAFKWE TAKIIQQLRA CGVLETVRIS AAGFPSRWLY PDFYMRYQLL
VYRSKLDKND MKLSCRNIVM KWIQDEDKYR FGNTQIFFRA GQVAFLEQVR ANLRKKYITI
VQSVVRRFVY RRQFLRIQKV INGIQKHARG YLARERTQKM REARAGLILS KYARGWLCRR
RYLRLRHSIS GIQTYARGML ARNKFHAMRD HYRAVQIQRF VRGALARRAY QKRRRNIIIC
QAAIRRFLAR RKFKRMKAEA KTISHMENKY MGLENKIISM QQRIDELNRD NSNLKHKTSE
ISVLKMKLEL KKTLEAEFKN VKAACQDKDK LIEALNKQLE AERDEKMQLL EENGHAQEEW
ISQKQTWRQE NEELRRQIDE IIDMAKNAEV NQRNQEDRML AEIDNRELNE AYQRAIKDKE
VIENENFMLK EELSRLTAGS FSLHARKASN ASSQNEDDVG YASAKNTLDI NRPPDLLSKN
YSYNDSTSLV VKLRSILEEE KQKHKVLQEQ YIKLSSRHKP TEDSFRTACR LAGRGT
//
